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Literature summary for 2.7.7.59 extracted from

  • Zhang, Y.; Pohlmann, E.L.; Roberts, G.P.
    GlnD is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity in the photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum (2005), J. Bacteriol., 187, 1254-1265.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information mutation and complementation studies show that the uridylyltransferase activity of the bifunctional uridylyltransferase/uridylyl-removing enzyme GlnD is localized to the N-terminal region Rhodospirillum rubrum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UTP + [protein-PII] Rhodospirillum rubrum GlnD plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of PII proteins, which in turn regulate a variety of other proteins. It is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity diphosphate + uridylyl-[protein-PII]
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?

Organism

Organism UniProt Comment Textmining
Rhodospirillum rubrum
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UTP + [protein-PII]
-
Rhodospirillum rubrum diphosphate + uridylyl-[protein-PII]
-
?
UTP + [protein-PII] GlnD plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of PII proteins, which in turn regulate a variety of other proteins. It is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity Rhodospirillum rubrum diphosphate + uridylyl-[protein-PII]
-
?

Synonyms

Synonyms Comment Organism
GlnD bifunctional uridylyltransferase/uridylyl-removing enzyme Rhodospirillum rubrum